6ACS

poly-cis-prenyltransferase

6ACS の概要

• エントリーDOI: 10.2210/pdb6acs/pdb
• 分子名称: Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific), CITRIC ACID, ISOPROPYL ALCOHOL, ... (5 entities in total)
• 機能のキーワード: citrate, complex, undecaprenyl pyrophosphate, synthase, upps, transferase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60209.88

構造登録者

Ko, T.-P.,Chen, Y. (登録日: 2018-07-27, 公開日: 2018-12-19, 最終更新日: 2023-11-22)

主引用文献

Ko, T.P.,Huang, C.H.,Lai, S.J.,Chen, Y.
Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii
Acta Crystallogr F Struct Biol Commun, 74:765-769, 2018

PubMed Abstract: Undecaprenyl pyrophosphate (UPP) is an important carrier of the oligosaccharide component in peptidoglycan synthesis. Inhibition of UPP synthase (UPPS) may be an effective strategy in combating the pathogen Acinetobacter baumannii, which has evolved to be multidrug-resistant. Here, A. baumannii UPPS (AbUPPS) was cloned, expressed, purified and crystallized, and its structure was determined by X-ray diffraction. Each chain of the dimeric protein folds into a central β-sheet with several surrounding α-helices, including one at the C-terminus. In the active site, two molecules of citrate interact with the side chains of the catalytic aspartate and serine. These observations may provide a structural basis for inhibitor design against AbUPPS.

PubMed: 30511669
DOI: 10.1107/S2053230X18012931

実験手法

X-RAY DIFFRACTION (1.81 Å)